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Isolation and functional analysis of a 24‐residue linear α‐helical antimicrobial peptide from Korean blackish cicada, Cryptotympana dubia (Homoptera)
Author(s) -
Park DooSang,
Leem Jae Yoon,
Suh Eun Young,
Hur Jang Hyun,
Oh HyunWoo,
Park HoYong
Publication year - 2007
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.20213
Subject(s) - biology , peptide , propidium iodide , antimicrobial , bacteria , microbiology and biotechnology , biochemistry , apoptosis , genetics , programmed cell death
A new antimicrobial peptide, cryptonin, was isolated and characterized from the adult Korean blackish cicada, Cryptotympana dubia . It consists of 24 amino acid residues and has a molecular weight of 2,704 Da on mass spectroscopy. The predicted α‐helical structure analysis and increased helix percent in 40% trifloroethanol of cryptonin suggests that it belongs to the typical linear α‐helix forming peptide. Binding of the biotin‐labeled cryptonin at the surface of E. coli cells and increased influx of propidium iodide in E. coli after cryptonin treatment indicates that it kills microbial cells by binding bacterial cell surfaces and disrupting the cell permeability. Cryptonin showed strong antibacterial (MIC 1.56–25 μg/ml) and antifungal (MIC 3.12–50 μg/ml) activities against tested bacteria and fungi including two antibiotic‐resistant bacterial strains; methicilin‐resistant S. aureus and vancomycin‐resistant Enterococci (MIC 25 μg/ml, each). Arch. Insect Biochem. Physiol. 66:204–213, 2007. © 2007 Wiley‐Liss, Inc.